Journal article

Molecular Characterization of Lipopolysaccharide Binding to Human α-1-Acid Glycoprotein.

Johnny X Huang, Mohammad AK Azad, Elizabeth Yuriev, Mark A Baker, Roger L Nation, Jian Li, Matthew A Cooper, Tony Velkov

J Lipids | Published : 2012


The ability of AGP to bind circulating lipopolysaccharide (LPS) in plasma is believed to help reduce the proinflammatory effect of bacterial lipid A molecules. Here, for the first time we have characterized human AGP binding characteristics of the LPS from a number of pathogenic Gram-negative bacteria: Escherichia coli, Salmonella typhimurium, Klebsiella pneumonia, Pseudomonas aeruginosa, and Serratia marcescens. The binding affinity and structure activity relationships (SAR) of the AGP-LPS interactions were characterized by surface plasma resonance (SPR). In order to dissect the contribution of the lipid A, core oligosaccharide and O-antigen polysaccharide components of LPS, the AGP binding..

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University of Melbourne Researchers


Awarded by NIAID NIH HHS

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